NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|688555680|ref|XP_009299893|]
View 

follistatin-A isoform X2 [Danio rerio]

Protein Classification

Kazal-type serine protease inhibitor family protein( domain architecture ID 11262404)

Kazal-type serine protease inhibitor family protein may function as a serine protease inhibitor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 120-167 1.45e-08

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 49.99  E-value: 1.45e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   120 VCAPDCSNVtwKGPVCGSDGKTYRDECALLKSKCKGHPDLEVQYQGKC 167
Cdd:smart00280   1 DCPEACPRE--YDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 272-319 2.07e-07

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 46.90  E-value: 2.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   272 VCAESCPesRSEEAVCASDNTTYPSECAMKQAACSLGVLLEVKHSGSC 319
Cdd:smart00280   1 DCPEACP--REYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 199-242 2.52e-07

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


:

Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 46.49  E-value: 2.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 688555680 199 CPEVMSPdqyLCGNDGIVYASACHLRRATCLLGRSIGVAYEGKC 242
Cdd:cd00104    1 CPKEYDP---VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 170-193 9.47e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


:

Pssm-ID: 128570  Cd Length: 24  Bit Score: 33.02  E-value: 9.47e-03
                           10        20
                   ....*....|....*....|....
gi 688555680   170 TCRDVLCPGSSTCVVDQTNNAYCV 193
Cdd:smart00274   1 SCRNVQCPFGKVCVVDKNGNARCV 24
 
Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 120-167 1.45e-08

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 49.99  E-value: 1.45e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   120 VCAPDCSNVtwKGPVCGSDGKTYRDECALLKSKCKGHPDLEVQYQGKC 167
Cdd:smart00280   1 DCPEACPRE--YDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 272-319 2.07e-07

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 46.90  E-value: 2.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   272 VCAESCPesRSEEAVCASDNTTYPSECAMKQAACSLGVLLEVKHSGSC 319
Cdd:smart00280   1 DCPEACP--REYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 98-169 2.21e-07

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 47.86  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688555680  98 CDNVDCGPGKRCKMNRRSKPRCVCAPDC-SNVTWKGPVCGSDGKTYRDECALLKSKC------KGHPD-----LEVQYQG 165
Cdd:cd01328    2 CENHHCGAGKVCEVDDENTPKCVCIDPCpEEVDDRRKVCTNDNETFDSDCELYRTRClckggkKGCRGpkyqhLHLDYYG 81


                 ....
gi 688555680 166 KCKK 169
Cdd:cd01328   82 ECKE 85
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 199-242 2.52e-07

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 46.49  E-value: 2.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 688555680 199 CPEVMSPdqyLCGNDGIVYASACHLRRATCLLGRSIGVAYEGKC 242
Cdd:cd00104    1 CPKEYDP---VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 195-242 3.42e-07

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 46.13  E-value: 3.42e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   195 CNRICPEVMSPdqyLCGNDGIVYASACHLRRATCLLGRSIGVAYEGKC 242
Cdd:smart00280   2 CPEACPREYDP---VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 280-319 1.10e-06

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 44.57  E-value: 1.10e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 688555680 280 SRSEEAVCASDNTTYPSECAMKQAACSLGVLLEVKHSGSC 319
Cdd:cd00104    2 PKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 273-319 1.16e-05

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.09  E-value: 1.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 688555680  273 CAESCPESRSEEaVCASDNTTYPSECAMKQAACSLGVLLE---VKHSGSC 319
Cdd:pfam07648   2 CNCQCPKTEYEP-VCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 121-167 7.05e-05

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 39.78  E-value: 7.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 688555680  121 CAPDCSNVTWKgPVCGSDGKTYRDECALLKSKCKGHPDLE---VQYQGKC 167
Cdd:pfam07648   2 CNCQCPKTEYE-PVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 195-242 2.94e-04

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 38.24  E-value: 2.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 688555680  195 CNRICPEVmsPDQYLCGNDGIVYASACHLRRATCLLGRSIG---VAYEGKC 242
Cdd:pfam07648   2 CNCQCPKT--EYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 170-193 9.47e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


Pssm-ID: 128570  Cd Length: 24  Bit Score: 33.02  E-value: 9.47e-03
                           10        20
                   ....*....|....*....|....
gi 688555680   170 TCRDVLCPGSSTCVVDQTNNAYCV 193
Cdd:smart00274   1 SCRNVQCPFGKVCVVDKNGNARCV 24
 
Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 120-167 1.45e-08

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 49.99  E-value: 1.45e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   120 VCAPDCSNVtwKGPVCGSDGKTYRDECALLKSKCKGHPDLEVQYQGKC 167
Cdd:smart00280   1 DCPEACPRE--YDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 272-319 2.07e-07

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 46.90  E-value: 2.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   272 VCAESCPesRSEEAVCASDNTTYPSECAMKQAACSLGVLLEVKHSGSC 319
Cdd:smart00280   1 DCPEACP--REYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 98-169 2.21e-07

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 47.86  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688555680  98 CDNVDCGPGKRCKMNRRSKPRCVCAPDC-SNVTWKGPVCGSDGKTYRDECALLKSKC------KGHPD-----LEVQYQG 165
Cdd:cd01328    2 CENHHCGAGKVCEVDDENTPKCVCIDPCpEEVDDRRKVCTNDNETFDSDCELYRTRClckggkKGCRGpkyqhLHLDYYG 81


                 ....
gi 688555680 166 KCKK 169
Cdd:cd01328   82 ECKE 85
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 199-242 2.52e-07

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 46.49  E-value: 2.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 688555680 199 CPEVMSPdqyLCGNDGIVYASACHLRRATCLLGRSIGVAYEGKC 242
Cdd:cd00104    1 CPKEYDP---VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 195-242 3.42e-07

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 46.13  E-value: 3.42e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688555680   195 CNRICPEVMSPdqyLCGNDGIVYASACHLRRATCLLGRSIGVAYEGKC 242
Cdd:smart00280   2 CPEACPREYDP---VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 133-167 4.96e-07

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 45.72  E-value: 4.96e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 688555680 133 PVCGSDGKTYRDECALLKSKCKGHPDLEVQYQGKC 167
Cdd:cd00104    7 PVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 280-319 1.10e-06

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 44.57  E-value: 1.10e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 688555680 280 SRSEEAVCASDNTTYPSECAMKQAACSLGVLLEVKHSGSC 319
Cdd:cd00104    2 PKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 273-319 1.16e-05

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.09  E-value: 1.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 688555680  273 CAESCPESRSEEaVCASDNTTYPSECAMKQAACSLGVLLE---VKHSGSC 319
Cdd:pfam07648   2 CNCQCPKTEYEP-VCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 248-307 1.36e-05

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 42.85  E-value: 1.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688555680 248 CDDIHCSAGKKCLWDaKMSRGRCaVCAESCPESRSE-EAVCASDNTTYPSECAMKQAACSL 307
Cdd:cd01328    2 CENHHCGAGKVCEVD-DENTPKC-VCIDPCPEEVDDrRKVCTNDNETFDSDCELYRTRCLC 60
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 121-167 7.05e-05

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 39.78  E-value: 7.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 688555680  121 CAPDCSNVTWKgPVCGSDGKTYRDECALLKSKCKGHPDLE---VQYQGKC 167
Cdd:pfam07648   2 CNCQCPKTEYE-PVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 195-242 2.94e-04

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 38.24  E-value: 2.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 688555680  195 CNRICPEVmsPDQYLCGNDGIVYASACHLRRATCLLGRSIG---VAYEGKC 242
Cdd:pfam07648   2 CNCQCPKT--EYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 171-230 1.17e-03

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 37.46  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688555680 171 CRDVLCPGSSTCVVDQTNNAYCVtCNRICPEVMSPDQYLCGNDGIVYASACHLRRATCLL 230
Cdd:cd01328    2 CENHHCGAGKVCEVDDENTPKCV-CIDPCPEEVDDRRKVCTNDNETFDSDCELYRTRCLC 60
MFS_SLCO4A_OATP4A cd17462
Solute carrier organic anion transporter 4A subfamily of the Major Facilitator Superfamily of ...
 193-259 1.53e-03

Solute carrier organic anion transporter 4A subfamily of the Major Facilitator Superfamily of transporters; The Solute carrier organic anion transporter 4A (SLCO4A), also called Organic anion-transporting polypeptide 4A (OATP4A), subfamily has one mammalian member, OATP4A1 (encoded by SLCO4A1). It is ubiquitously expressed and it mediates the Na(+)-independent transport of the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and other organic anions such as estrone sulfate and taurocholate. OATP4A1 is the most abundantly expressed transporter colorectal cancer (CRC) and its role in the transport of estrone sulfate, which is used in hormone replacement therapy (HRT), affects the outcome of the treatment. The SLCO4A/OATP4A subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341020 [Multi-domain]  Cd Length: 427  Bit Score: 40.20  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688555680 193 VTCNRIC---PEVMSPdqyLCGNDGIVYASACH--LRRATCLLGRSIGVAYEGKCIKAKSCDDIHCSAGKKC 259
Cdd:cd17462  325 ALCNADCrclEEIYSP---VCGADGLMYYSPCHagCSEAYSDIRNGQKVYQDCSCVAGNLSVGFGEASAGKC 393
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 133-167 2.89e-03

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 34.95  E-value: 2.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 688555680 133 PVCGSDGKTYRDECALLKSKCKGHPDLEVQYQGKC 167
Cdd:cd01327   11 PVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 133-167 3.93e-03

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 34.95  E-value: 3.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 688555680  133 PVCGSDGKTYRDECALLKSKCKGHPDLEVQYQGKC 167
Cdd:pfam00050  15 PVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 170-193 9.47e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


Pssm-ID: 128570  Cd Length: 24  Bit Score: 33.02  E-value: 9.47e-03
                           10        20
                   ....*....|....*....|....
gi 688555680   170 TCRDVLCPGSSTCVVDQTNNAYCV 193
Cdd:smart00274   1 SCRNVQCPFGKVCVVDKNGNARCV 24
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH